Salehzada T, Silhol M, Steff A M, Lebleu B, Bisbal C
Laboratoire de Biochimie des Protéines, URA Centre National de la Recherche Scientifique 1191, Université de Montpellier II Sciences et Techniques du Languedoc, France.
J Biol Chem. 1993 Apr 15;268(11):7733-40.
The subunit composition of RNase L, a key enzyme in the interferon system, has been characterized. RNase L was purified from human Daudi cells on a column of 2-5A-Sepharose and used to immunize Balb/c mice. A specific monoclonal antibody which recognizes a protein of 80 kDa has been isolated. This protein has been characterized and shown to be an RNA-binding protein with nuclease activity which is associated with, but distinct from, the 80-kDa 2-5A-binding protein known previously as RNase L. It is therefore proposed that the 2-5A-dependent RNase L is a complex of two distinct subunits: an 80-kDa RNA-binding protein (i.e. the catalytic subunit) and an 80-kDa 2-5A-binding protein (i.e. the regulatory subunit).